The carbohydrate binding site recognizes (β-1,4) linked N-acetylglucosamine oligomers, preferring chitobiose or chitotriose over a single N-acetylglucosamine residue. This lectin binds well in the acidic pH range but its affinity decreases above pH 8.0.
DSL also binds well to N-acetyllactosamine and oligomers containing repeating N-acetyllactosamine sequences. A branched pentasaccharide including two N-acetyllactosamine disaccharides linked to mannose (β-1,6) and (β-1,2) was reported to be the most potent inhibitor of agglutination.
Biotinylated Datura stramonium lectin has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide.
